scholarly journals Paeoniflorin, the Main Active Ingredient of Shuyu Capsule, Inhibits Cav1.2 and Regulates Calmodulin/Calmodulin-Dependent Protein Kinase II Signalling

2017 ◽  
Vol 2017 ◽  
pp. 1-10 ◽  
Author(s):  
Chunhong Song ◽  
Jieqiong Wang ◽  
Dongmei Gao ◽  
Yanhong Yu ◽  
Fang Li ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Active Ingredient ◽  
Signalling Pathway ◽  
Patch Clamps ◽  
Dependent Protein Kinase ◽  
Voltage Gated ◽  
Signalling Molecules ◽  
Protein Kinase Ii ◽  
Intracellular Ca ◽  
Dependent Protein

The aim of this study was to explore the mechanism underlying the antidepression activity of paeoniflorin, the main active ingredient of paeony extract and Shuyu capsules, and determine its effect on the calmodulin/calmodulin-dependent protein kinase II (CaM/CaMKII) signalling pathway and on the possible target, the voltage-gated calcium channel (Cav). Rats at the nonacceptance stage were selected for premenstrual syndrome (PMS) depression modelling. Behavioural assays were used for model testing. Rats were given Shuyu capsules, paeony extract, and bupleurum. Western blot analysis was used to assess the expression levels of calcium voltage-gated channel subunit alpha 1 C (CACNA1C), brain-derived neurotrophic factor, and CaM/CaMKII signalling pathway proteins. Intracellular Ca2+ concentration in CHO cell line was measured using Fluo-4-AM and whole-cell patch clamps. The PMS depression model was successfully established and demonstrated that Shuyu can mitigate depressive behaviour in a rat PMS model. Paeony extract did not affect CACNA1C protein expression in rat hippocampi but did affect Cav1.2-mediated CaM/CaMKII signalling pathways. Paeoniflorin significantly inhibited KCl-induced increases in intracellular Ca2+ concentration and Cav1.2 current density. Further, it may function via the CaM/CaMKII pathway and its downstream signalling molecules by regulating Cav1.2, thus playing an important role in the treatment and alleviation of affective disorders.

scholarly journals Ca 2+ /Calmodulin-Dependent Protein Kinase II–Based Regulation of Voltage-Gated Na + Channel in Cardiac Disease

Circulation ◽  
2012 ◽  
Vol 126 (17) ◽  
pp. 2084-2094 ◽  
Author(s):  
Olha M. Koval ◽  
Jedidiah S. Snyder ◽  
Roseanne M. Wolf ◽  
Ryan E. Pavlovicz ◽  
Patric Glynn ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cardiac Disease ◽  
Na Channel ◽  
Dependent Protein Kinase ◽  
Voltage Gated ◽  
Protein Kinase Ii ◽  
Dependent Protein

scholarly journals Ca2+-induced loss of Ca2+/calmodulin-dependent protein kinase II activity in pancreatic β-cells

1998 ◽  
Vol 274 (4) ◽  
pp. E708-E715 ◽  
Author(s):  
Peter M. Jones ◽  
Shanta J. Persaud
Keyword(s):  
Insulin Secretion ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Β Cells ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Exogenous Substrate ◽  
Protein Kinase Ii ◽  
Intracellular Ca ◽  
Dependent Protein

Elevations in intracellular Ca2+ in electrically permeabilized islets of Langerhans produced rapid insulin secretory responses from β-cells, but the Ca2+-induced secretion was not maintained and was irrespective of the pattern of administration of elevated Ca2+. Ca2+-insensitive β-cells responded normally to activators of protein kinase C or cAMP-dependent kinase with increased insulin secretion. The loss of secretory responsiveness to Ca2+ was paralleled by a reduction in Ca2+-induced protein phosphorylation. This was caused by a reduction in Ca2+/calmodulin-dependent protein kinase II (CaMK II) activity in the desensitized cells, as assessed by measuring the phosphorylation of a CaMK II-specific exogenous substrate, autocamtide-2. The Ca2+-induced reductions in kinase activity and protein phosphorylation were not dependent on the activation of Ca2+-dependent protein kinases and were not caused by the activation of phosphoprotein phosphatases or of Ca2+-activated proteases. The concomitant reductions in CaMK II activity and Ca2+-induced insulin secretion suggest that the activation of CaMK II is required for normal insulin secretory responses to increased intracellular Ca2+ concentrations.

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